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Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery.
J Biol Chem 2005; 280(13):13004-11JB

Abstract

Members of the Oxa1/YidC family are involved in the biogenesis of membrane proteins. In bacteria, YidC catalyzes the insertion and assembly of proteins of the inner membrane. Mitochondria of animals, fungi, and plants harbor two distant homologues of YidC, Oxa1 and Cox18/Oxa2. Oxa1 plays a pivotal role in the integration of mitochondrial translation products into the inner membrane of mitochondria. It contains a C-terminal ribosome-binding domain that physically interacts with mitochondrial ribosomes to facilitate the co-translational insertion of nascent membrane proteins. The molecular function of Cox18/Oxa2 is not well understood. Employing a functional complementation approach with mitochondria-targeted versions of YidC we show that YidC is able to functionally replace both Oxa1 and Cox18/Oxa2. However, to integrate mitochondrial translation products into the inner membrane of mitochondria, the ribosome-binding domain of Oxa1 has to be appended onto YidC. On the contrary, the fusion of the ribosome-binding domain onto YidC prevents its ability to complement COX18 mutants suggesting an indispensable post-translational activity of Cox18/Oxa2. Our observations suggest that during evolution of mitochondria from their bacterial ancestors the two descendents of YidC functionally segregated to perform two distinct activities, one co-translational and one post-translational.

Authors+Show Affiliations

Institut für Physiologische Chemie, Universität München, Butenandtstrasse 5, 81377 München, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15654078

Citation

Preuss, Marc, et al. "Evolution of Mitochondrial Oxa Proteins From Bacterial YidC. Inherited and Acquired Functions of a Conserved Protein Insertion Machinery." The Journal of Biological Chemistry, vol. 280, no. 13, 2005, pp. 13004-11.
Preuss M, Ott M, Funes S, et al. Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery. J Biol Chem. 2005;280(13):13004-11.
Preuss, M., Ott, M., Funes, S., Luirink, J., & Herrmann, J. M. (2005). Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery. The Journal of Biological Chemistry, 280(13), pp. 13004-11.
Preuss M, et al. Evolution of Mitochondrial Oxa Proteins From Bacterial YidC. Inherited and Acquired Functions of a Conserved Protein Insertion Machinery. J Biol Chem. 2005 Apr 1;280(13):13004-11. PubMed PMID: 15654078.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery. AU - Preuss,Marc, AU - Ott,Martin, AU - Funes,Soledad, AU - Luirink,Joen, AU - Herrmann,Johannes M, Y1 - 2005/01/14/ PY - 2005/1/18/pubmed PY - 2005/5/14/medline PY - 2005/1/18/entrez SP - 13004 EP - 11 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 280 IS - 13 N2 - Members of the Oxa1/YidC family are involved in the biogenesis of membrane proteins. In bacteria, YidC catalyzes the insertion and assembly of proteins of the inner membrane. Mitochondria of animals, fungi, and plants harbor two distant homologues of YidC, Oxa1 and Cox18/Oxa2. Oxa1 plays a pivotal role in the integration of mitochondrial translation products into the inner membrane of mitochondria. It contains a C-terminal ribosome-binding domain that physically interacts with mitochondrial ribosomes to facilitate the co-translational insertion of nascent membrane proteins. The molecular function of Cox18/Oxa2 is not well understood. Employing a functional complementation approach with mitochondria-targeted versions of YidC we show that YidC is able to functionally replace both Oxa1 and Cox18/Oxa2. However, to integrate mitochondrial translation products into the inner membrane of mitochondria, the ribosome-binding domain of Oxa1 has to be appended onto YidC. On the contrary, the fusion of the ribosome-binding domain onto YidC prevents its ability to complement COX18 mutants suggesting an indispensable post-translational activity of Cox18/Oxa2. Our observations suggest that during evolution of mitochondria from their bacterial ancestors the two descendents of YidC functionally segregated to perform two distinct activities, one co-translational and one post-translational. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/15654078/Evolution_of_mitochondrial_oxa_proteins_from_bacterial_YidC__Inherited_and_acquired_functions_of_a_conserved_protein_insertion_machinery_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=15654078 DB - PRIME DP - Unbound Medicine ER -